The enzyme pyridoxal phosphatase[1][2][3] (EC 3.1.3.74) catalyzes the reaction
| Pyridoxal phosphatase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.1.3.74 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
- pyridoxal 5′-phosphate + H2O pyridoxal + phosphate
This enzyme belongs to the family of hydrolases, specifically those acting on phosphoric monoester bonds. The systematic name is pyridoxal-5′-phosphate phosphohydrolase. Other names in common use include vitamine B6 (pyridoxine) phosphatase, PLP phosphatase, vitamin B6-phosphate phosphatase, and PNP phosphatase. This enzyme participates in vitamin B6 metabolism.
Structural studies
editAs of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 2CFR, 2CFS, 2CFT, 2OYC, 2P27, and 2P69.
References
edit- ^ Fonda ML (1992). "Purification and characterization of vitamin B6-phosphate phosphatase from human erythrocytes". J. Biol. Chem. 267 (22): 15978–83. doi:10.1016/S0021-9258(19)49630-0. PMID 1322411.
- ^ Fonda ML, Zhang YN (1995). "Kinetic mechanism and divalent metal activation of human erythrocyte pyridoxal phosphatase". Arch. Biochem. Biophys. 320 (2): 345–52. doi:10.1016/0003-9861(95)90018-7. PMID 7625842.
- ^ Jang, Y.M.; Kim, DW; Kang, TC; Won, MH; Baek, NI; Moon, BJ; Choi, SY; Kwon, OS (2003). "Human pyridoxal phosphatase. Molecular cloning, functional expression, and tissue distribution". J. Biol. Chem. 278 (50): 50040–6. doi:10.1074/jbc.M309619200. PMID 14522954.
